We attempted to study intermediates that may be formed during ATP hydrolysis of the heat shock related protein, ATPase. Crystals of one particular mutant of ATPase was used to perform time-resolved Laue diffraction experiments, in which the rate of hydrolysis is significantly reduced to 100-1000 sec in solution. The data sets were collected at several time increments after ATP was introduced to the crystal via a flow cell. The data were of good quality and completeness, however, the difference maps showed no indication of structural change.